AUH antibody
Principal name
AUH antibody
Alternative names for AUH antibody
mitochondrial Methylglutaconyl-CoA hydratase, AU-specific RNA-binding enoyl-CoA hydratase, AU-binding protein/enoyl-CoA hydratase
Ncbi ID
9606, NP_001689, NP_057918.2, NM_001698, NP_001689.1, NM_016709
Available reactivities
Available hosts
Available applications
Enzyme Immunoassay (E), Western blot / Immunoblot (WB), Paraffin Sections (P)
Background of AUH antibody
AU-specific RNA-binding enoyl-CoA hydratase (AUH) protein binds to the AU-rich element (ARE), a common element found in the 3\' UTR of rapidly decaying mRNA such as c-fos, c-myc and granulocyte/ macrophage colony stimulating factor. ARE elements are involved in directing RNA to rapid degradation and deadenylation. AUH is also homologous to enol-CoA hydratase, an enzyme involved in fatty acid degradation, and has been shown to have intrinsic hydratase enzymatic activity. AUH is thus a bifunctional chimera between RNA binding and metabolic enzyme activity. A possible subcellular localization in the mitochondria has been demonstrated for the mouse homolog of this protein which shares 92% identity with the human protein. It has been suggested that AUH may have a novel role as a mitochondrial located AU-binding protein. Human AUH is expressed as a single mRNA species of 1.8 kb, and translated as a 40-kDa precursor protein which is subsequently processed to a 32-kDa mature form.AU-specific RNA-binding enoyl-CoA hydratase (AUH) protein binds to the AU-rich element (ARE), a common element found in the 3\' UTR of rapidly decaying mRNA such as c-fos, c-myc and granulocyte/ macrophage colony stimulating factor. ARE elements are involved in directing RNA to rapid degradation and deadenylation. AUH is also homologous to enol-CoA hydratase, an enzyme involved in fatty acid degradation, and has been shown to have intrinsic hydratase enzymatic activity. AUH is thus a bifunctional chimera between RNA binding and metabolic enzyme activity. A possible subcellular localization in the mitochondria has been demonstrated for the mouse homolog of this protein which shares 92% identity with the human protein. It has been suggested that AUH may have a novel role as a mitochondrial located AU-binding protein. Human AUH is expressed as a single mRNA species of 1.8 kb, and translated as a 40-kDa precursor protein which is subsequently processed to a 32-kDa mature form.
General readings
Kurimoto K, et al. (2009). Proteins 75(2):360-72.
Mack M., et al. (2006). FEBS J. 273(9):2012-22.





Proteins & Growth Factors
| Catalog No. | Species | Pres. | Purity | Source | |
|---|---|---|---|---|---|
| TP318117 | AUH |
||||
| Recombinant protein of human AU RNA binding protein/enoyl-Coenzyme A hydratase (AUH), nuclear gene encoding mitochondrial protein | |||||
![]() |
Human | > 80 % Preparation: Recombint protein was captured through anti-DDK affinity column followed by conventiol chromatography steps. Purity Detail: > 80% as determined by SDS-PAGE and Coomassie blue staining. |
HEK293 cells |
20 µg /
€748.00
|
|
| OriGene Technologies, Inc. | |||||
Lysates
| Catalog No. | ||
|---|---|---|
| LY419798 | AUH overexpression lysate |
|
![]() |
0.1 mg /
€295.00
|
|
| OriGene Technologies, Inc. |
Human Lenti ORF Particles
| Catalog No. | ||
|---|---|---|
| RC218117L1V | Lenti ORF particles, AUH (Myc-DDK tagged) - Human AU RNA binding protein/enoyl-CoA hydratase (AUH), nuclear gene encoding mitochondrial protein , 200 uL, >10^7 TU/mL |
|
![]() |
200 µl /
€860.00
|
|
| OriGene Technologies, Inc. | ||
Mouse Lenti ORF Particles
| Catalog No. | ||
|---|---|---|
| MR204476L2V | Lenti ORF particles, Auh (GFP-tagged) - Mouse AU RNA binding protein/enoyl-coenzyme A hydratase (Auh), nuclear gene encoding mitochondrial protein, 200 uL, >10^7 TU/mL |
|
![]() |
200 µl /
€930.00
|
|
| OriGene Technologies, Inc. | ||
| MR204476L1V | Lenti ORF particles, Auh (Myc-DDK-tagged) - Mouse AU RNA binding protein/enoyl-coenzyme A hydratase (Auh), nuclear gene encoding mitochondrial protein, 200 uL, >10^7 TU/mL |
|
![]() |
200 µl /
€830.00
|
|
| OriGene Technologies, Inc. | ||





